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Determination of the accessible surface of globular proteins by means of tritium planigraphy

✍ Scribed by A. V. Volynskaya; E. A. Kasumov; E. N. Bogascheva; A. V. Shishkov; V. I. Goldanskii

Publisher
Springer
Year
1994
Tongue
English
Weight
467 KB
Volume
23
Category
Article
ISSN
1432-1017

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✦ Synopsis

Results are presented for proteins with known three-dimensional structure (lysozyme, myoglobin, ribonuclease), which show that the probability of label incorporation upon bombardment by "hot" tritium atoms may be quantitatively linked with the surface area of the protein accessible to water molecules. Possible deviations from simple linear dependency caused by particular mechanisms of label introduction are discussed. The data obtained in experiments with model systems were used to determine the accessible surface area of human serum albumin, for which structural data is not sufficiently accurate to allow estimation of accessible surface area. Experimental data correlate reasonably well with estimations based on conventional concepts of the relationship between accessible surface area and molecular weight for globular proteins.

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